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Conserved domains on  [gi|17551340|ref|NP_509274|]
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Cuticle collagen dpy-7 [Caenorhabditis elegans]

Protein Classification

cuticular collagen family protein( domain architecture ID 10661013)

cuticular collagen family protein is a structural macromolecule of the extracellular matrix containing triple helix domains that form tight interactions and stabilize supramolecular aggregates

Gene Ontology:  GO:0042302|GO:0005581
PubMed:  1916105|21421911

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
gly_rich_SclB super family cl45768
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 145-206 6.44e-12

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


The actual alignment was detected with superfamily member NF038329:

Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 65.70  E-value: 6.44e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17551340  145 PAGPPGTRGPQGEVGRPGQTGESGHPGLPGRPGKPGRVGDAGPQGEPGEQGEPGIKGPPGDD 206
Cdd:NF038329 130 PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEK 191
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 11-62 2.36e-07

Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is found in the N-terminal region of nematode cuticle collagens. Cuticle is a tough elastic structure secreted by hypodermal cells and is primarily composed of collagen proteins.


:

Pssm-ID: 198156  Cd Length: 53  Bit Score: 46.69  E-value: 2.36e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 17551340     11 VAKATVSLSIASVLILGAVLTMLSIQLDEAHERLQNRMGSFKFVARNIWHDI 62
Cdd:smart01088   2 VAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 145-206 6.44e-12

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 65.70  E-value: 6.44e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17551340  145 PAGPPGTRGPQGEVGRPGQTGESGHPGLPGRPGKPGRVGDAGPQGEPGEQGEPGIKGPPGDD 206
Cdd:NF038329 130 PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEK 191
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 109-233 6.47e-11

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 62.62  E-value: 6.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551340  109 SGEPGMDGANGRPGKPGLDGLDVPLDPEPafpcvicPAGPPGTRGPQGEVGRPGQTGESGHPGLPGRPGKPGRVGDAGPQ 188
Cdd:NF038329 143 TGPAGPAGPPGPQGERGEKGPAGPQGEAG-------PQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPD 215

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 17551340  189 GEPGEQGEPGIKGPPGDDSIGGTGIKGPPGPPGPRGPKGPPGSNG 233
Cdd:NF038329 216 GEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDG 260
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 112-206 2.00e-10

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 61.46  E-value: 2.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551340  112 PGMDGANGRPGKPGLDGLDVPLDPEPafpcvicPAGPPGTRGPQGEVGRPGQTGESGHPGLPGRPGKPGRVGDAGPQGEP 191
Cdd:NF038329 229 PAGDGQQGPDGDPGPTGEDGPQGPDG-------PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKD 301

                         90
                 ....*....|....*
gi 17551340  192 GEQGEPGIKGPPGDD 206
Cdd:NF038329 302 GKDGQNGKDGLPGKD 316
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 106-205 2.44e-10

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 61.07  E-value: 2.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551340  106 PGVSGEPGMDGANGRPGKPGLDGLDVP-----LDPEPAFPCVICPAGPPGTRGPQGEVGRPGQTGESGHPGLPGRPGKPG 180
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPqgergEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207

                         90       100
                 ....*....|....*....|....*
gi 17551340  181 RVGDAGPQGEPGEQGEPGIKGPPGD 205
Cdd:NF038329 208 PAGPAGPDGEAGPAGEDGPAGPAGD 232
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 147-203 2.50e-10

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 55.19  E-value: 2.50e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 17551340   147 GPPGTRGPQGEVGRPGQTGESGHPGLPGRPGKPGRVGDAGPQGEPGEQGEPGIKGPP 203
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 11-62 2.36e-07

Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is found in the N-terminal region of nematode cuticle collagens. Cuticle is a tough elastic structure secreted by hypodermal cells and is primarily composed of collagen proteins.


Pssm-ID: 198156  Cd Length: 53  Bit Score: 46.69  E-value: 2.36e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 17551340     11 VAKATVSLSIASVLILGAVLTMLSIQLDEAHERLQNRMGSFKFVARNIWHDI 62
Cdd:smart01088   2 VAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
Col_cuticle_N pfam01484
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 14-62 2.39e-06

Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is found in the N-terminal region of nematode cuticle collagens, see pfam01391. Cuticle is a tough elastic structure secreted by hypodermal cells and is primarily composed of collagen proteins.


Pssm-ID: 460226  Cd Length: 50  Bit Score: 43.99  E-value: 2.39e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 17551340    14 ATVSLSIASVLILGAVLTMLSIQLDEAHERLQNRMGSFKFVARNIWHDI 62
Cdd:pfam01484   2 VAVAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAWNEM 50
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 110-191 8.75e-06

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 46.82  E-value: 8.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551340  110 GEPGMDGANGRPGKPGLDGLDvpldpepafpcvicpaGPPGTRGPQGEVGRPGQTGESGHPGLPGRPGKPGRVGDAGPQG 189
Cdd:NF038329 275 GKDGERGPVGPAGKDGQNGKD----------------GLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338


                 ..
gi 17551340  190 EP 191
Cdd:NF038329 339 KP 340
 
Name Accession Description Interval E-value
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 145-206 6.44e-12

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 65.70  E-value: 6.44e-12
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17551340  145 PAGPPGTRGPQGEVGRPGQTGESGHPGLPGRPGKPGRVGDAGPQGEPGEQGEPGIKGPPGDD 206
Cdd:NF038329 130 PAGEQGPRGDRGETGPAGPAGPPGPQGERGEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEK 191
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 109-233 6.47e-11

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 62.62  E-value: 6.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551340  109 SGEPGMDGANGRPGKPGLDGLDVPLDPEPafpcvicPAGPPGTRGPQGEVGRPGQTGESGHPGLPGRPGKPGRVGDAGPQ 188
Cdd:NF038329 143 TGPAGPAGPPGPQGERGEKGPAGPQGEAG-------PQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQGPAGPAGPD 215

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 17551340  189 GEPGEQGEPGIKGPPGDDSIGGTGIKGPPGPPGPRGPKGPPGSNG 233
Cdd:NF038329 216 GEAGPAGEDGPAGPAGDGQQGPDGDPGPTGEDGPQGPDGPAGKDG 260
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 112-206 2.00e-10

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 61.46  E-value: 2.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551340  112 PGMDGANGRPGKPGLDGLDVPLDPEPafpcvicPAGPPGTRGPQGEVGRPGQTGESGHPGLPGRPGKPGRVGDAGPQGEP 191
Cdd:NF038329 229 PAGDGQQGPDGDPGPTGEDGPQGPDG-------PAGKDGPRGDRGEAGPDGPDGKDGERGPVGPAGKDGQNGKDGLPGKD 301

                         90
                 ....*....|....*
gi 17551340  192 GEQGEPGIKGPPGDD 206
Cdd:NF038329 302 GKDGQNGKDGLPGKD 316
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 106-205 2.44e-10

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 61.07  E-value: 2.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551340  106 PGVSGEPGMDGANGRPGKPGLDGLDVP-----LDPEPAFPCVICPAGPPGTRGPQGEVGRPGQTGESGHPGLPGRPGKPG 180
Cdd:NF038329 128 AGPAGEQGPRGDRGETGPAGPAGPPGPqgergEKGPAGPQGEAGPQGPAGKDGEAGAKGPAGEKGPQGPRGETGPAGEQG 207

                         90       100
                 ....*....|....*....|....*
gi 17551340  181 RVGDAGPQGEPGEQGEPGIKGPPGD 205
Cdd:NF038329 208 PAGPAGPDGEAGPAGEDGPAGPAGD 232
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 147-203 2.50e-10

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 55.19  E-value: 2.50e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 17551340   147 GPPGTRGPQGEVGRPGQTGESGHPGLPGRPGKPGRVGDAGPQGEPGEQGEPGIKGPP 203
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 145-197 2.92e-08

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 49.41  E-value: 2.92e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 17551340   145 PAGPPGTRGPQGEVGRPGQTGESGHPGLPGRPGKPGRVGDAGPQGEPGEQGEP 197
Cdd:pfam01391   5 PPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPGPP 57
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 145-198 3.70e-08

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 49.03  E-value: 3.70e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 17551340   145 PAGPPGTRGPQGEVGRPGQTGESGHPGLPGRPGKPGRVGDAGPQGEPGEQGEPG 198
Cdd:pfam01391   2 PPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
Col_cuticle_N smart01088
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 11-62 2.36e-07

Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is found in the N-terminal region of nematode cuticle collagens. Cuticle is a tough elastic structure secreted by hypodermal cells and is primarily composed of collagen proteins.


Pssm-ID: 198156  Cd Length: 53  Bit Score: 46.69  E-value: 2.36e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 17551340     11 VAKATVSLSIASVLILGAVLTMLSIQLDEAHERLQNRMGSFKFVARNIWHDI 62
Cdd:smart01088   2 VAYVAVAVSTVAVLSALVTLPSIYNDIQSFQSELLDEMDEFKARADDAWNEM 53
Col_cuticle_N pfam01484
Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is ...
 14-62 2.39e-06

Nematode cuticle collagen N-terminal domain; The function of this domain is unknown. It is found in the N-terminal region of nematode cuticle collagens, see pfam01391. Cuticle is a tough elastic structure secreted by hypodermal cells and is primarily composed of collagen proteins.


Pssm-ID: 460226  Cd Length: 50  Bit Score: 43.99  E-value: 2.39e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 17551340    14 ATVSLSIASVLILGAVLTMLSIQLDEAHERLQNRMGSFKFVARNIWHDI 62
Cdd:pfam01484   2 VAVAFSTVAILSSLITLPSIYNDIQELQSEVLDEMDEFKARSDDAWNEM 50
gly_rich_SclB NF038329
LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like ...
 110-191 8.75e-06

LPXTG-anchored collagen-like adhesin Scl2/SclB; SclB (or Scl2 - streptococcal collagen-like protein 2) is an LPXTG-anchored surface-anchored adhesin with a variable-length region of triple helix-forming collagen-like Gly-Xaa-Xaa repeats.


Pssm-ID: 468478 [Multi-domain]  Cd Length: 440  Bit Score: 46.82  E-value: 8.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17551340  110 GEPGMDGANGRPGKPGLDGLDvpldpepafpcvicpaGPPGTRGPQGEVGRPGQTGESGHPGLPGRPGKPGRVGDAGPQG 189
Cdd:NF038329 275 GKDGERGPVGPAGKDGQNGKD----------------GLPGKDGKDGQNGKDGLPGKDGKDGQPGKDGLPGKDGKDGQPG 338


                 ..
gi 17551340  190 EP 191
Cdd:NF038329 339 KP 340
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 165-204 1.44e-04

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 39.01  E-value: 1.44e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 17551340   165 GESGHPGLPGRPGKPGRVGDAGPQGEPGEQGEPGIKGPPG 204
Cdd:pfam01391   1 GPPGPPGPPGPPGPPGPPGPPGPPGPPGPPGEPGPPGPPG 40
Collagen pfam01391
Collagen triple helix repeat (20 copies); Members of this family belong to the collagen ...
 110-180 4.94e-04

Collagen triple helix repeat (20 copies); Members of this family belong to the collagen superfamily. Collagens are generally extracellular structural proteins involved in formation of connective tissue structure. The alignment contains 20 copies of the G-X-Y repeat that forms a triple helix. The first position of the repeat is glycine, the second and third positions can be any residue but are frequently proline and hydroxy-proline. Collagens are post translationally modified by proline hydroxylase to form the hydroxy-proline residues. Defective hydroxylation is the cause of scurvy. Some members of the collagen superfamily are not involved in connective tissue structure but share the same triple helical structure. The family includes bacterial collagen-like triple-helix repeat proteins.


Pssm-ID: 460189 [Multi-domain]  Cd Length: 57  Bit Score: 37.47  E-value: 4.94e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17551340   110 GEPGMDGANGRPGkpgldgldvpldpepafpcvicPAGPPGTRGPQGEVGRPGQTGESGHPGLPGRPGKPG 180
Cdd:pfam01391   7 GPPGPPGPPGPPG----------------------PPGPPGPPGPPGEPGPPGPPGPPGPPGPPGAPGAPG 55
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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